ID K9XY92_STAC7 Unreviewed; 494 AA.
AC K9XY92;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sta7437_3573 {ECO:0000313|EMBL:AFZ37071.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ37071.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; CP003653; AFZ37071.1; -; Genomic_DNA.
DR RefSeq; WP_015194733.1; NC_019748.1.
DR AlphaFoldDB; K9XY92; -.
DR STRING; 111780.Sta7437_3573; -.
DR KEGG; scs:Sta7437_3573; -.
DR PATRIC; fig|111780.3.peg.3700; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_3; -.
DR Proteomes; UP000010473; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFZ37071.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Transferase {ECO:0000313|EMBL:AFZ37071.1}.
FT DOMAIN 131..200
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 274..491
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 494 AA; 56472 MW; A4F18C9787A0FE7A CRC64;
MNQLLIFDQR EYVIINQNLI VLQRSTTAQK FAESPQTLVP GQDIRLSFPE LIGLENVLTQ
ILNQEQEFFS LETIARHVNN KTNLYFNLLI KKLGNNLIIF LEDTTEIILL KQSLVQQINE
AEVLVSTLKR FEDCTKKILT SMGDVLFITT PSGEIEQINQ AAKKVFGYNQ NELVAKTIDF
IVKNENFDHE KVYNYLLKNR NKVQKIDAIC QTKSGELREI EFSCSIVQTE IKEFFNCVYI
GRDITARKQA ETEILQALQK EKELREIKSR FISLASHEFR NPLSSILIAA NFLAENKNNI
SQEDWDFYLK TINTAAQNMQ SLVEDILVIS KTEEGKLTFN PGLLNLNKFC QRLIKELEIT
ANKKNILFST NVEHLVIWSD EKILKLIINN LLSNAIKYSP QEENIEFKIL YFAEQEIVQI
IIQDYGIGIP VEARKHLFDS FYRANNVGDI PGTGLGLSIV KKAVDLHGGK IELNSKLGLG
TIITVILPVN HQSC
//
